data_4228 #Corrected using PDB structure: 1XBL_ # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 6 Y HA 3.89 4.62 # 13 K HA 2.57 3.93 # 52 A HA 2.70 3.61 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 70 H CA 59.02 53.22 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 72 A CB 18.39 26.30 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 11 V N 110.01 124.03 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.01 -0.08 -0.11 0.27 -0.29 0.04 # #bmr4228.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4228.str file): #HA CA CB CO N HN #N/A -0.10 -0.10 +0.27 -0.29 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.04 +/-0.17 +/-0.21 +/-0.20 +/-0.51 +/-0.10 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.586 0.940 0.990 0.705 0.580 0.223 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.154 0.709 0.887 0.850 2.139 0.443 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structures (20) of the J-Domain (residues 1-77) of the Escherichia coli n-terminal fragment (residues 1-104) of the molecular chaperone DNAJ ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang K. . . 2 Flanagan J. M. . 3 Prestegard J. H. . stop_ _BMRB_accession_number 4228 _BMRB_flat_file_name bmr4228.str _Entry_type new _Submission_date 1998-08-20 _Accession_date 1998-08-20 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 524 '13C chemical shifts' 376 '15N chemical shifts' 92 stop_ loop_ _Related_BMRB_accession_number _Relationship 4227 "the N-terminal fragment (residues 1-78)" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; The influence of c-terminal extension on the structure of the j-domain in e. coli dnaj" ; _Citation_status 'published' _Citation_type journal _MEDLINE_UI_code . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang K. . . 2 Flanagan J. . . 3 Prestegard J. . . stop_ _Journal_abbreviation "Protein Sci." _Journal_volume . _Page_first 5587 _Page_last 5596 _Year 1998 loop_ _Keyword "chaperone" "heat shock" "protein folding" "DNAK" stop_ save_ ################################## # Molecular system description # ################################## save_system_DNAJ _Saveframe_category molecular_system _Mol_system_name DNAJ _Abbreviation_common DNAJ _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DNAJ $DNAJ stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1BQ0 . . stop_ save_ ######################## # Monomeric polymers # ######################## save_DNAJ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DNAJ _Name_variant . _Abbreviation_common DNAJ _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 103 _Mol_residue_sequence ; AKQDYYEILGVSKTAEEREI RKAYKRLAMKYHPDRNQGDK EAEAKFKEIKEAYEVLTDSQ KRAAYDQYGHAAFEQGGMGG GGFGGGADFSDIFGDVFGDI FGG ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 LYS 3 GLN 4 ASP 5 TYR 6 TYR 7 GLU 8 ILE 9 LEU 10 GLY 11 VAL 12 SER 13 LYS 14 THR 15 ALA 16 GLU 17 GLU 18 ARG 19 GLU 20 ILE 21 ARG 22 LYS 23 ALA 24 TYR 25 LYS 26 ARG 27 LEU 28 ALA 29 MET 30 LYS 31 TYR 32 HIS 33 PRO 34 ASP 35 ARG 36 ASN 37 GLN 38 GLY 39 ASP 40 LYS 41 GLU 42 ALA 43 GLU 44 ALA 45 LYS 46 PHE 47 LYS 48 GLU 49 ILE 50 LYS 51 GLU 52 ALA 53 TYR 54 GLU 55 VAL 56 LEU 57 THR 58 ASP 59 SER 60 GLN 61 LYS 62 ARG 63 ALA 64 ALA 65 TYR 66 ASP 67 GLN 68 TYR 69 GLY 70 HIS 71 ALA 72 ALA 73 PHE 74 GLU 75 GLN 76 GLY 77 GLY 78 MET 79 GLY 80 GLY 81 GLY 82 GLY 83 PHE 84 GLY 85 GLY 86 GLY 87 ALA 88 ASP 89 PHE 90 SER 91 ASP 92 ILE 93 PHE 94 GLY 95 ASP 96 VAL 97 PHE 98 GLY 99 ASP 100 ILE 101 PHE 102 GLY 103 GLY stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1BQZ "J-Domain (Residues 1-77) Of The EscherichiaColi N-Terminal Fragment (Residues 1-78) Of TheMolecular Chaperone Dnaj, Nmr, 20 Structures" 133.77 77 100 100 3e-38 PDB 1BQ0 "J-Domain (Residues 1-77) Of The EscherichiaColi N-Terminal Fragment (Residues 1-104) Of TheMolecular Chaperone Dnaj, Nmr, 20 Structures" 100.00 103 100 100 4e-55 PDB 1XBL "Nmr Structure Of The J-Domain (Residues 2-76)In The Escherichia Coli N-Terminal Fragment (Residues2-108) Of The Molecular Chaperone Dnaj, 20 Structures" 96.26 107 100 100 4e-55 DBJ BAB96590.1 "DnaJ protein. [Escherichia coli]" 27.39 376 100 100 4e-55 DBJ BAB33438.1 "DnaJ protein [Escherichia coli O157:H7]" 27.39 376 99 100 9e-55 GenBank AAA00009.1 "DnaJ [Escherichia coli]" 27.39 376 100 100 4e-55 GenBank AAA23693.1 "heat shock protein dnaJ" 27.39 376 100 100 4e-55 GenBank AAC73126.1 "chaperone with DnaK; heat shock protein;heat shock protein (Hsp40), co-chaperone with DnaK[Escherichia coli K12]" 27.39 376 100 100 4e-55 GenBank AAP15561.1 "chaperone with DnaK; heat shock protein[Shigella flexneri 2a str. 2457T]" 27.39 376 100 100 4e-55 GenBank AAN41681.1 "chaperone with DnaK; heat shock protein[Shigella flexneri 2a str. 301]" 26.68 386 100 100 4e-55 PIR HHECDJ "heat shock protein dnaJ - Escherichia coli(strain K-12)" 27.39 376 100 100 4e-55 PIR G85481 "chaperone with DnaK, heat shock protein[imported] - Escherichia coli (strain O157:H7, substrainEDL933)" 27.39 376 99 100 9e-55 PIR G90630 "DnaJ protein [imported] - Escherichia coli(strain O157:H7, substrain RIMD 0509952)" 27.39 376 99 100 9e-55 REF NP_414556.1 "chaperone with DnaK; heat shockprotein; heat shock protein (Hsp40), co-chaperone withDnaK [Escherichia coli K12]" 27.39 376 100 100 4e-55 REF NP_835756.1 "chaperone with DnaK; heat shockprotein [Shigella flexneri 2a str. 2457T]" 27.39 376 100 100 4e-55 REF NP_285707.1 "chaperone with DnaK; heat shockprotein [Escherichia coli O157:H7 EDL933]" 27.39 376 99 100 9e-55 REF NP_308042.1 "DnaJ [Escherichia coli O157:H7]" 27.39 376 99 100 9e-55 REF NP_705974.1 "chaperone with DnaK; heat shockprotein [Shigella flexneri 2a str. 301]" 26.68 386 100 100 4e-55 SWISS-PROT P08622 "DNAJ_ECOLI Chaperone protein dnaJ (Heat shockprotein J) (HSP40)" 27.39 376 100 100 4e-55 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Plasmid $DNAJ "Escherichia coli" 562 Bacteria Proteobacteria Escherichia coli "pDnaJ(1-104)11d" stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $DNAJ 'recombinant technology' "Escherichia coli" Escherichia coli MgT7 T7 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DNAJ . mM . phosphate 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer GE _Model Omega _Field_strength 500 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 . n/a temperature 303 . K 'ionic strength' 50 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio . H 1 . ppm . . . . . . . . C 13 . ppm . . . . . . . . N 15 . ppm . . . . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name DNAJ loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 ALA CA C 51.50 . . 2 1 ALA HA H 4.11 . . 3 1 ALA CB C 19.30 . . 4 1 ALA HB H 1.53 . . 5 2 LYS C C 175.67 . . 6 2 LYS CA C 56.20 . . 7 2 LYS HA H 4.24 . . 8 2 LYS CB C 32.70 . . 9 2 LYS HB2 H 1.32 . . 10 2 LYS HB3 H 1.53 . . 11 2 LYS HG2 H 1.74 . . 12 2 LYS HG3 H 1.74 . . 13 2 LYS HD2 H 1.55 . . 14 2 LYS HD3 H 1.47 . . 15 2 LYS CG C 24.60 . . 16 2 LYS CD C 28.90 . . 17 3 GLN N N 121.91 . . 18 3 GLN H H 8.48 . . 19 3 GLN C C 175.37 . . 20 3 GLN CA C 55.50 . . 21 3 GLN HA H 4.30 . . 22 3 GLN CB C 30.30 . . 23 3 GLN HB2 H 1.92 . . 24 3 GLN HB3 H 2.03 . . 25 3 GLN HG2 H 2.45 . . 26 3 GLN HG3 H 2.45 . . 27 3 GLN HE21 H 7.65 . . 28 3 GLN HE22 H 6.89 . . 29 3 GLN CG C 34.30 . . 30 3 GLN NE2 N 112.00 . . 31 4 ASP N N 122.71 . . 32 4 ASP H H 8.84 . . 33 4 ASP C C 176.67 . . 34 4 ASP CA C 53.50 . . 35 4 ASP HA H 4.57 . . 36 4 ASP CB C 42.90 . . 37 4 ASP HB2 H 2.77 . . 38 4 ASP HB3 H 3.14 . . 39 5 TYR N N 121.61 . . 40 5 TYR H H 7.34 . . 41 5 TYR C C 176.37 . . 42 5 TYR CA C 58.30 . . 43 5 TYR HA H 4.33 . . 44 5 TYR CB C 38.10 . . 45 5 TYR HB2 H 1.94 . . 46 5 TYR HB3 H 2.66 . . 47 5 TYR HD1 H 6.02 . . 48 5 TYR HD2 H 6.02 . . 49 5 TYR HE1 H 6.61 . . 50 5 TYR HE2 H 6.61 . . 51 5 TYR CD1 C 130.70 . . 52 5 TYR CD2 C 130.70 . . 53 5 TYR CE1 C 119.00 . . 54 5 TYR CE2 C 119.00 . . 55 6 TYR N N 114.91 . . 56 6 TYR H H 7.67 . . 57 6 TYR C C 178.17 . . 58 6 TYR CA C 62.10 . . 59 6 TYR HA H 3.90 . . 60 6 TYR CB C 35.30 . . 61 6 TYR HB2 H 3.21 . . 62 6 TYR HB3 H 3.25 . . 63 6 TYR HD1 H 7.38 . . 64 6 TYR HD2 H 7.38 . . 65 6 TYR HE1 H 6.93 . . 66 6 TYR HE2 H 6.93 . . 67 6 TYR CD1 C 134.20 . . 68 6 TYR CD2 C 134.20 . . 69 6 TYR CE1 C 118.80 . . 70 6 TYR CE2 C 118.80 . . 71 7 GLU N N 119.21 . . 72 7 GLU H H 7.97 . . 73 7 GLU C C 180.07 . . 74 7 GLU CA C 58.90 . . 75 7 GLU HA H 4.18 . . 76 7 GLU CB C 29.70 . . 77 7 GLU HB2 H 2.32 . . 78 7 GLU HB3 H 2.24 . . 79 7 GLU HG2 H 2.58 . . 80 7 GLU HG3 H 2.58 . . 81 7 GLU CG C 36.40 . . 82 8 ILE N N 119.51 . . 83 8 ILE H H 8.24 . . 84 8 ILE C C 176.87 . . 85 8 ILE CA C 64.60 . . 86 8 ILE HA H 3.72 . . 87 8 ILE CB C 37.60 . . 88 8 ILE HB H 1.96 . . 89 8 ILE HG12 H 1.14 . . 90 8 ILE HG13 H 1.70 . . 91 8 ILE HG2 H 0.88 . . 92 8 ILE HD1 H 0.87 . . 93 8 ILE CG1 C 29.10 . . 94 8 ILE CG2 C 18.10 . . 95 8 ILE CD1 C 13.90 . . 96 9 LEU N N 114.71 . . 97 9 LEU H H 6.98 . . 98 9 LEU C C 175.57 . . 99 9 LEU CA C 54.50 . . 100 9 LEU HA H 4.37 . . 101 9 LEU CB C 42.90 . . 102 9 LEU HB2 H 1.62 . . 103 9 LEU HB3 H 1.80 . . 104 9 LEU HG H 1.94 . . 105 9 LEU HD1 H 0.86 . . 106 9 LEU HD2 H 1.03 . . 107 9 LEU CG C 27.20 . . 108 9 LEU CD1 C 26.90 . . 109 9 LEU CD2 C 23.50 . . 110 10 GLY N N 108.11 . . 111 10 GLY H H 8.06 . . 112 10 GLY C C 175.07 . . 113 10 GLY CA C 46.40 . . 114 10 GLY HA2 H 3.95 . . 115 11 VAL N N 110.01 . . 116 11 VAL H H 7.89 . . 117 11 VAL C C 174.27 . . 118 11 VAL CA C 58.00 . . 119 11 VAL HA H 4.83 . . 120 11 VAL CB C 34.90 . . 121 11 VAL HB H 2.32 . . 122 11 VAL HG1 H 1.04 . . 123 11 VAL HG2 H 0.83 . . 124 11 VAL CG1 C 18.90 . . 125 11 VAL CG2 C 21.70 . . 126 12 SER N N 114.81 . . 127 12 SER H H 8.34 . . 128 12 SER C C 174.37 . . 129 12 SER CA C 57.00 . . 130 12 SER HA H 4.43 . . 131 12 SER CB C 64.10 . . 132 12 SER HB2 H 3.75 . . 133 12 SER HB3 H 3.97 . . 134 13 LYS N N 120.41 . . 135 13 LYS H H 8.19 . . 136 13 LYS C C 176.67 . . 137 13 LYS CA C 57.60 . . 138 13 LYS HA H 2.58 . . 139 13 LYS CB C 32.10 . . 140 13 LYS HB2 H 1.47 . . 141 13 LYS HB3 H 1.47 . . 142 13 LYS HG2 H 1.12 . . 143 13 LYS HG3 H 1.24 . . 144 13 LYS HD2 H 1.58 . . 145 13 LYS HD3 H 1.58 . . 146 13 LYS HE2 H 2.99 . . 147 13 LYS HE3 H 2.99 . . 148 13 LYS CG C 24.80 . . 149 13 LYS CD C 29.90 . . 150 13 LYS CE C 41.90 . . 151 14 THR N N 104.11 . . 152 14 THR H H 7.35 . . 153 14 THR C C 174.37 . . 154 14 THR CA C 59.70 . . 155 14 THR HA H 4.23 . . 156 14 THR CB C 67.90 . . 157 14 THR HB H 4.59 . . 158 14 THR HG2 H 1.07 . . 159 14 THR CG2 C 21.40 . . 160 15 ALA N N 124.41 . . 161 15 ALA H H 7.59 . . 162 15 ALA C C 177.67 . . 163 15 ALA CA C 52.80 . . 164 15 ALA HA H 4.21 . . 165 15 ALA CB C 19.30 . . 166 15 ALA HB H 1.52 . . 167 16 GLU N N 120.01 . . 168 16 GLU H H 9.01 . . 169 16 GLU C C 177.67 . . 170 16 GLU CA C 55.30 . . 171 16 GLU HA H 4.58 . . 172 16 GLU CB C 31.00 . . 173 16 GLU HB2 H 2.13 . . 174 16 GLU HB3 H 2.46 . . 175 16 GLU HG2 H 2.47 . . 176 16 GLU HG3 H 2.53 . . 177 16 GLU CG C 36.60 . . 178 17 GLU N N 123.31 . . 179 17 GLU H H 9.25 . . 180 17 GLU C C 178.17 . . 181 17 GLU CA C 60.90 . . 182 17 GLU HA H 3.86 . . 183 17 GLU CB C 29.30 . . 184 17 GLU HB2 H 2.31 . . 185 17 GLU HB3 H 2.31 . . 186 17 GLU HG2 H 2.20 . . 187 17 GLU HG3 H 2.34 . . 188 17 GLU CG C 36.30 . . 189 18 ARG N N 115.91 . . 190 18 ARG H H 9.01 . . 191 18 ARG C C 178.47 . . 192 18 ARG CA C 59.60 . . 193 18 ARG HA H 4.10 . . 194 18 ARG CB C 29.60 . . 195 18 ARG HB2 H 1.90 . . 196 18 ARG HB3 H 2.04 . . 197 18 ARG HG2 H 1.65 . . 198 18 ARG HG3 H 1.65 . . 199 18 ARG CG C 26.80 . . 200 19 GLU N N 119.01 . . 201 19 GLU H H 7.47 . . 202 19 GLU C C 178.97 . . 203 19 GLU CA C 58.90 . . 204 19 GLU HA H 4.18 . . 205 19 GLU CB C 29.80 . . 206 19 GLU HB2 H 2.26 . . 207 19 GLU HB3 H 2.41 . . 208 19 GLU HG2 H 2.40 . . 209 19 GLU HG3 H 2.47 . . 210 19 GLU CG C 36.60 . . 211 20 ILE N N 122.01 . . 212 20 ILE H H 7.86 . . 213 20 ILE C C 176.97 . . 214 20 ILE CA C 65.90 . . 215 20 ILE HA H 3.64 . . 216 20 ILE CB C 37.90 . . 217 20 ILE HB H 2.01 . . 218 20 ILE HG12 H 0.92 . . 219 20 ILE HG13 H 1.78 . . 220 20 ILE HG2 H 0.86 . . 221 20 ILE HD1 H 0.83 . . 222 20 ILE CG1 C 30.20 . . 223 20 ILE CG2 C 17.90 . . 224 20 ILE CD1 C 13.40 . . 225 21 ARG N N 117.91 . . 226 21 ARG H H 8.64 . . 227 21 ARG C C 178.27 . . 228 21 ARG CA C 60.50 . . 229 21 ARG HA H 4.27 . . 230 21 ARG CB C 29.00 . . 231 21 ARG HB2 H 1.90 . . 232 21 ARG HB3 H 2.05 . . 233 21 ARG HG2 H 1.21 . . 234 21 ARG HG3 H 1.53 . . 235 21 ARG HD2 H 3.29 . . 236 21 ARG HD3 H 3.41 . . 237 21 ARG CG C 27.10 . . 238 21 ARG CD C 43.00 . . 239 22 LYS N N 119.11 . . 240 22 LYS H H 7.87 . . 241 22 LYS C C 178.37 . . 242 22 LYS CA C 59.70 . . 243 22 LYS HA H 4.04 . . 244 22 LYS CB C 32.50 . . 245 22 LYS HB2 H 2.00 . . 246 22 LYS HB3 H 2.00 . . 247 22 LYS HG2 H 1.70 . . 248 22 LYS HG3 H 1.49 . . 249 22 LYS HD2 H 1.76 . . 250 22 LYS HD3 H 1.76 . . 251 22 LYS HE2 H 3.00 . . 252 22 LYS HE3 H 3.00 . . 253 22 LYS CG C 25.10 . . 254 22 LYS CD C 29.40 . . 255 22 LYS CE C 41.70 . . 256 23 ALA N N 122.11 . . 257 23 ALA H H 8.06 . . 258 23 ALA C C 179.57 . . 259 23 ALA CA C 55.00 . . 260 23 ALA HA H 4.18 . . 261 23 ALA CB C 18.50 . . 262 23 ALA HB H 1.70 . . 263 24 TYR N N 116.71 . . 264 24 TYR H H 8.40 . . 265 24 TYR C C 175.57 . . 266 24 TYR CA C 61.40 . . 267 24 TYR HA H 3.97 . . 268 24 TYR CB C 38.70 . . 269 24 TYR HB2 H 2.82 . . 270 24 TYR HB3 H 2.88 . . 271 24 TYR HD1 H 6.41 . . 272 24 TYR HD2 H 6.41 . . 273 24 TYR HE1 H 6.24 . . 274 24 TYR HE2 H 6.24 . . 275 24 TYR CD1 C 132.50 . . 276 24 TYR CD2 C 132.50 . . 277 24 TYR CE1 C 117.50 . . 278 24 TYR CE2 C 117.50 . . 279 25 LYS N N 117.41 . . 280 25 LYS H H 8.13 . . 281 25 LYS C C 178.67 . . 282 25 LYS CA C 59.50 . . 283 25 LYS HA H 3.54 . . 284 25 LYS CB C 31.90 . . 285 25 LYS HB2 H 1.88 . . 286 25 LYS HB3 H 1.88 . . 287 25 LYS HG2 H 1.43 . . 288 25 LYS HG3 H 1.62 . . 289 25 LYS HD2 H 1.70 . . 290 25 LYS HD3 H 1.70 . . 291 25 LYS HE2 H 3.00 . . 292 25 LYS HE3 H 3.00 . . 293 25 LYS CG C 25.30 . . 294 25 LYS CD C 29.10 . . 295 25 LYS CE C 41.70 . . 296 26 ARG N N 116.81 . . 297 26 ARG H H 7.65 . . 298 26 ARG C C 179.07 . . 299 26 ARG CA C 58.90 . . 300 26 ARG HA H 4.06 . . 301 26 ARG CB C 30.10 . . 302 26 ARG HB2 H 1.98 . . 303 26 ARG HB3 H 1.98 . . 304 26 ARG HG2 H 1.59 . . 305 26 ARG HG3 H 1.77 . . 306 26 ARG HD2 H 3.28 . . 307 26 ARG HD3 H 3.28 . . 308 26 ARG CG C 27.30 . . 309 26 ARG CD C 43.30 . . 310 27 LEU N N 120.41 . . 311 27 LEU H H 8.03 . . 312 27 LEU C C 178.47 . . 313 27 LEU CA C 57.50 . . 314 27 LEU HA H 4.14 . . 315 27 LEU CB C 42.40 . . 316 27 LEU HB2 H 1.96 . . 317 27 LEU HB3 H 1.60 . . 318 27 LEU HG H 1.82 . . 319 27 LEU HD1 H 1.16 . . 320 27 LEU HD2 H 1.06 . . 321 27 LEU CG C 26.70 . . 322 27 LEU CD1 C 26.60 . . 323 27 LEU CD2 C 22.80 . . 324 28 ALA N N 122.11 . . 325 28 ALA H H 9.17 . . 326 28 ALA C C 179.27 . . 327 28 ALA CA C 54.90 . . 328 28 ALA HA H 3.90 . . 329 28 ALA CB C 16.90 . . 330 28 ALA HB H 1.00 . . 331 29 MET N N 113.51 . . 332 29 MET H H 7.32 . . 333 29 MET C C 177.37 . . 334 29 MET CA C 57.50 . . 335 29 MET HA H 4.14 . . 336 29 MET CB C 32.20 . . 337 29 MET HB2 H 1.99 . . 338 29 MET HB3 H 2.11 . . 339 29 MET HG2 H 2.70 . . 340 29 MET HG3 H 2.60 . . 341 29 MET HE H 2.06 . . 342 29 MET CG C 31.90 . . 343 29 MET CE C 16.60 . . 344 30 LYS N N 117.91 . . 345 30 LYS H H 7.32 . . 346 30 LYS C C 177.47 . . 347 30 LYS CA C 58.30 . . 348 30 LYS HA H 3.98 . . 349 30 LYS CB C 32.70 . . 350 30 LYS HB2 H 1.59 . . 351 30 LYS HB3 H 1.65 . . 352 30 LYS HG2 H 1.16 . . 353 30 LYS HG3 H 0.68 . . 354 30 LYS HD2 H 1.52 . . 355 30 LYS HD3 H 1.38 . . 356 30 LYS HE2 H 2.86 . . 357 30 LYS HE3 H 2.86 . . 358 30 LYS CG C 24.40 . . 359 30 LYS CD C 29.30 . . 360 30 LYS CE C 41.90 . . 361 31 TYR N N 114.51 . . 362 31 TYR H H 7.84 . . 363 31 TYR C C 173.47 . . 364 31 TYR CA C 58.30 . . 365 31 TYR HA H 4.51 . . 366 31 TYR CB C 38.70 . . 367 31 TYR HB2 H 2.48 . . 368 31 TYR HB3 H 3.38 . . 369 31 TYR HD1 H 7.10 . . 370 31 TYR HD2 H 7.10 . . 371 31 TYR HE1 H 6.79 . . 372 31 TYR HE2 H 6.79 . . 373 31 TYR CD1 C 133.30 . . 374 31 TYR CD2 C 133.30 . . 375 31 TYR CE1 C 118.40 . . 376 31 TYR CE2 C 118.40 . . 377 32 HIS N N 119.41 . . 378 32 HIS H H 7.62 . . 379 32 HIS CA C 55.50 . . 380 32 HIS HA H 4.16 . . 381 32 HIS CB C 29.90 . . 382 32 HIS HB2 H 2.82 . . 383 32 HIS HB3 H 3.14 . . 384 33 PRO C C 177.57 . . 385 33 PRO CA C 64.70 . . 386 33 PRO HA H 4.22 . . 387 33 PRO CB C 31.70 . . 388 33 PRO HB2 H 1.89 . . 389 33 PRO HB3 H 2.18 . . 390 33 PRO HG2 H 1.67 . . 391 33 PRO HG3 H 1.67 . . 392 33 PRO HD2 H 2.59 . . 393 33 PRO HD3 H 2.89 . . 394 33 PRO CG C 27.00 . . 395 33 PRO CD C 50.10 . . 396 34 ASP N N 119.11 . . 397 34 ASP H H 9.68 . . 398 34 ASP C C 176.97 . . 399 34 ASP CA C 55.40 . . 400 34 ASP HA H 4.52 . . 401 34 ASP CB C 40.30 . . 402 34 ASP HB2 H 2.70 . . 403 34 ASP HB3 H 2.70 . . 404 35 ARG N N 117.31 . . 405 35 ARG H H 7.96 . . 406 35 ARG C C 175.57 . . 407 35 ARG CA C 55.50 . . 408 35 ARG HA H 4.45 . . 409 35 ARG CB C 30.70 . . 410 35 ARG HB2 H 1.73 . . 411 35 ARG HB3 H 1.98 . . 412 35 ARG HG2 H 1.77 . . 413 35 ARG HG3 H 1.60 . . 414 35 ARG HD2 H 3.18 . . 415 35 ARG HD3 H 3.18 . . 416 35 ARG CG C 27.00 . . 417 35 ARG CD C 43.00 . . 418 36 ASN N N 118.41 . . 419 36 ASN H H 7.95 . . 420 36 ASN C C 174.67 . . 421 36 ASN CA C 52.40 . . 422 36 ASN HA H 4.89 . . 423 36 ASN CB C 39.80 . . 424 36 ASN HB2 H 2.55 . . 425 36 ASN HB3 H 2.81 . . 426 36 ASN HD21 H 6.99 . . 427 36 ASN HD22 H 7.72 . . 428 36 ASN ND2 N 114.20 . . 429 37 GLN N N 120.11 . . 430 37 GLN H H 8.50 . . 431 37 GLN C C 176.67 . . 432 37 GLN CA C 57.10 . . 433 37 GLN HA H 4.22 . . 434 37 GLN CB C 28.40 . . 435 37 GLN HB2 H 2.04 . . 436 37 GLN HB3 H 2.15 . . 437 37 GLN HG2 H 2.41 . . 438 37 GLN HG3 H 2.41 . . 439 37 GLN HE21 H 7.53 . . 440 37 GLN HE22 H 6.83 . . 441 37 GLN CG C 33.80 . . 442 37 GLN NE2 N 111.90 . . 443 38 GLY N N 110.21 . . 444 38 GLY H H 8.77 . . 445 38 GLY HA2 H 3.91 . . 446 38 GLY HA3 H 4.04 . . 447 39 ASP N N 119.51 . . 448 39 ASP H H 7.85 . . 449 39 ASP C C 176.47 . . 450 39 ASP CA C 53.30 . . 451 39 ASP HA H 4.77 . . 452 39 ASP CB C 41.50 . . 453 39 ASP HB2 H 2.65 . . 454 39 ASP HB3 H 2.99 . . 455 40 LYS N N 125.31 . . 456 40 LYS H H 8.82 . . 457 40 LYS C C 178.87 . . 458 40 LYS CA C 58.50 . . 459 40 LYS HA H 4.16 . . 460 40 LYS CB C 31.90 . . 461 40 LYS HB2 H 1.88 . . 462 40 LYS HB3 H 1.88 . . 463 40 LYS HG2 H 1.57 . . 464 40 LYS HG3 H 1.62 . . 465 40 LYS HD2 H 1.75 . . 466 40 LYS HD3 H 1.75 . . 467 40 LYS HE2 H 3.06 . . 468 40 LYS HE3 H 3.06 . . 469 40 LYS CG C 24.70 . . 470 40 LYS CD C 28.60 . . 471 40 LYS CE C 41.90 . . 472 41 GLU N N 120.71 . . 473 41 GLU H H 8.45 . . 474 41 GLU C C 178.37 . . 475 41 GLU CA C 58.80 . . 476 41 GLU HA H 4.28 . . 477 41 GLU CB C 28.90 . . 478 41 GLU HB2 H 2.18 . . 479 41 GLU HB3 H 2.18 . . 480 41 GLU HG2 H 2.32 . . 481 41 GLU HG3 H 2.37 . . 482 41 GLU CG C 36.40 . . 483 42 ALA N N 123.01 . . 484 42 ALA H H 8.07 . . 485 42 ALA C C 179.07 . . 486 42 ALA CA C 54.90 . . 487 42 ALA HA H 4.14 . . 488 42 ALA CB C 17.90 . . 489 42 ALA HB H 1.57 . . 490 43 GLU N N 116.81 . . 491 43 GLU H H 8.04 . . 492 43 GLU C C 178.47 . . 493 43 GLU CA C 59.20 . . 494 43 GLU HA H 4.13 . . 495 43 GLU CB C 29.50 . . 496 43 GLU HB2 H 2.16 . . 497 43 GLU HB3 H 2.16 . . 498 43 GLU HG2 H 2.29 . . 499 43 GLU HG3 H 2.46 . . 500 43 GLU CG C 36.00 . . 501 44 ALA N N 121.41 . . 502 44 ALA H H 7.86 . . 503 44 ALA C C 180.47 . . 504 44 ALA CA C 53.60 . . 505 44 ALA HA H 4.14 . . 506 44 ALA CB C 17.90 . . 507 44 ALA HB H 1.57 . . 508 45 LYS N N 118.51 . . 509 45 LYS H H 8.05 . . 510 45 LYS C C 178.77 . . 511 45 LYS CA C 58.30 . . 512 45 LYS HA H 4.05 . . 513 45 LYS CB C 31.30 . . 514 45 LYS HB2 H 1.38 . . 515 45 LYS HB3 H 1.64 . . 516 45 LYS HG2 H 1.33 . . 517 45 LYS HG3 H 1.26 . . 518 45 LYS HD2 H 1.52 . . 519 45 LYS HD3 H 1.52 . . 520 45 LYS CG C 24.60 . . 521 45 LYS CD C 28.20 . . 522 46 PHE N N 119.11 . . 523 46 PHE H H 8.66 . . 524 46 PHE C C 176.37 . . 525 46 PHE CA C 61.00 . . 526 46 PHE HA H 4.13 . . 527 46 PHE CB C 38.50 . . 528 46 PHE HB2 H 3.07 . . 529 46 PHE HB3 H 3.19 . . 530 46 PHE HD1 H 7.08 . . 531 46 PHE HD2 H 7.08 . . 532 46 PHE HE1 H 7.23 . . 533 46 PHE HE2 H 7.23 . . 534 46 PHE CD1 C 131.60 . . 535 46 PHE CD2 C 131.60 . . 536 46 PHE CE1 C 131.50 . . 537 46 PHE CE2 C 131.50 . . 538 47 LYS N N 117.61 . . 539 47 LYS H H 8.02 . . 540 47 LYS C C 178.97 . . 541 47 LYS CA C 59.80 . . 542 47 LYS HA H 3.83 . . 543 47 LYS CB C 32.00 . . 544 47 LYS HB2 H 1.94 . . 545 47 LYS HB3 H 1.94 . . 546 47 LYS HG2 H 1.47 . . 547 47 LYS HG3 H 1.72 . . 548 47 LYS HD2 H 1.76 . . 549 47 LYS HD3 H 1.76 . . 550 47 LYS HE2 H 3.03 . . 551 47 LYS HE3 H 3.03 . . 552 47 LYS CG C 25.30 . . 553 47 LYS CD C 29.40 . . 554 47 LYS CE C 42.40 . . 555 48 GLU N N 118.01 . . 556 48 GLU H H 7.50 . . 557 48 GLU C C 178.27 . . 558 48 GLU CA C 58.70 . . 559 48 GLU HA H 4.22 . . 560 48 GLU CB C 29.60 . . 561 48 GLU HB2 H 2.25 . . 562 48 GLU HB3 H 2.16 . . 563 48 GLU HG2 H 2.34 . . 564 48 GLU HG3 H 2.51 . . 565 48 GLU CG C 36.20 . . 566 49 ILE N N 119.51 . . 567 49 ILE H H 7.85 . . 568 49 ILE C C 176.67 . . 569 49 ILE CA C 64.90 . . 570 49 ILE HA H 3.63 . . 571 49 ILE CB C 38.10 . . 572 49 ILE HB H 1.83 . . 573 49 ILE HG12 H 1.14 . . 574 49 ILE HG13 H 1.69 . . 575 49 ILE HG2 H 0.96 . . 576 49 ILE HD1 H 0.83 . . 577 49 ILE CG1 C 29.10 . . 578 49 ILE CG2 C 17.80 . . 579 49 ILE CD1 C 15.50 . . 580 50 LYS N N 120.51 . . 581 50 LYS H H 8.23 . . 582 50 LYS C C 177.37 . . 583 50 LYS CA C 60.00 . . 584 50 LYS HA H 3.80 . . 585 50 LYS CB C 32.10 . . 586 50 LYS HB2 H 1.66 . . 587 50 LYS HB3 H 1.66 . . 588 50 LYS HG2 H 1.30 . . 589 50 LYS HG3 H 1.30 . . 590 50 LYS HD2 H 1.58 . . 591 50 LYS HD3 H 1.65 . . 592 50 LYS HE2 H 3.03 . . 593 50 LYS HE3 H 3.03 . . 594 50 LYS CG C 24.70 . . 595 50 LYS CD C 29.50 . . 596 50 LYS CE C 42.40 . . 597 51 GLU N N 118.61 . . 598 51 GLU H H 7.69 . . 599 51 GLU C C 176.97 . . 600 51 GLU CA C 59.10 . . 601 51 GLU HA H 3.82 . . 602 51 GLU CB C 29.40 . . 603 51 GLU HB2 H 2.02 . . 604 51 GLU HB3 H 2.02 . . 605 51 GLU HG2 H 1.95 . . 606 51 GLU HG3 H 2.25 . . 607 51 GLU CG C 35.70 . . 608 52 ALA N N 118.51 . . 609 52 ALA H H 7.55 . . 610 52 ALA C C 177.87 . . 611 52 ALA CA C 54.30 . . 612 52 ALA HA H 2.71 . . 613 52 ALA CB C 18.60 . . 614 52 ALA HB H 1.38 . . 615 53 TYR N N 116.41 . . 616 53 TYR H H 8.12 . . 617 53 TYR C C 176.67 . . 618 53 TYR CA C 60.70 . . 619 53 TYR HA H 3.62 . . 620 53 TYR CB C 39.10 . . 621 53 TYR HB2 H 2.61 . . 622 53 TYR HB3 H 2.61 . . 623 53 TYR HD1 H 6.36 . . 624 53 TYR HD2 H 6.36 . . 625 53 TYR HE1 H 6.43 . . 626 53 TYR HE2 H 6.43 . . 627 53 TYR CD1 C 132.40 . . 628 53 TYR CD2 C 132.40 . . 629 53 TYR CE1 C 118.20 . . 630 53 TYR CE2 C 118.20 . . 631 54 GLU N N 119.51 . . 632 54 GLU H H 8.24 . . 633 54 GLU C C 178.07 . . 634 54 GLU CA C 58.90 . . 635 54 GLU HA H 3.28 . . 636 54 GLU CB C 28.70 . . 637 54 GLU HB2 H 1.65 . . 638 54 GLU HB3 H 1.79 . . 639 54 GLU HG2 H 2.09 . . 640 54 GLU HG3 H 2.47 . . 641 54 GLU CG C 36.60 . . 642 55 VAL N N 116.91 . . 643 55 VAL H H 7.30 . . 644 55 VAL C C 175.97 . . 645 55 VAL CA C 65.90 . . 646 55 VAL HA H 3.35 . . 647 55 VAL CB C 31.20 . . 648 55 VAL HB H 1.16 . . 649 55 VAL HG1 H 0.53 . . 650 55 VAL HG2 H 0.47 . . 651 55 VAL CG1 C 22.40 . . 652 55 VAL CG2 C 20.70 . . 653 56 LEU N N 110.41 . . 654 56 LEU H H 7.63 . . 655 56 LEU C C 177.27 . . 656 56 LEU CA C 56.30 . . 657 56 LEU HA H 3.77 . . 658 56 LEU CB C 41.80 . . 659 56 LEU HB2 H 1.26 . . 660 56 LEU HB3 H 1.52 . . 661 56 LEU HG H 1.51 . . 662 56 LEU HD1 H 0.16 . . 663 56 LEU HD2 H 0.32 . . 664 56 LEU CG C 27.00 . . 665 56 LEU CD1 C 25.00 . . 666 56 LEU CD2 C 22.00 . . 667 57 THR N N 103.21 . . 668 57 THR H H 7.19 . . 669 57 THR C C 173.27 . . 670 57 THR CA C 61.40 . . 671 57 THR HA H 4.10 . . 672 57 THR CB C 68.80 . . 673 57 THR HB H 4.14 . . 674 57 THR HG2 H 0.77 . . 675 57 THR CG2 C 22.00 . . 676 58 ASP N N 123.41 . . 677 58 ASP H H 7.05 . . 678 58 ASP C C 175.27 . . 679 58 ASP CA C 52.90 . . 680 58 ASP HA H 4.86 . . 681 58 ASP CB C 43.00 . . 682 58 ASP HB2 H 2.53 . . 683 58 ASP HB3 H 2.99 . . 684 59 SER N N 120.71 . . 685 59 SER H H 9.03 . . 686 59 SER C C 176.67 . . 687 59 SER CA C 62.30 . . 688 59 SER HA H 4.05 . . 689 59 SER CB C 62.50 . . 690 59 SER HB2 H 3.98 . . 691 59 SER HB3 H 3.98 . . 692 60 GLN N N 120.41 . . 693 60 GLN H H 8.19 . . 694 60 GLN C C 178.97 . . 695 60 GLN CA C 58.80 . . 696 60 GLN HA H 4.28 . . 697 60 GLN CB C 28.60 . . 698 60 GLN HB2 H 2.25 . . 699 60 GLN HB3 H 2.25 . . 700 60 GLN HG2 H 2.54 . . 701 60 GLN HG3 H 2.42 . . 702 60 GLN HE21 H 6.83 . . 703 60 GLN HE22 H 7.70 . . 704 60 GLN CG C 34.30 . . 705 60 GLN NE2 N 111.40 . . 706 61 LYS N N 122.51 . . 707 61 LYS H H 8.55 . . 708 61 LYS C C 178.47 . . 709 61 LYS CA C 60.20 . . 710 61 LYS HA H 4.29 . . 711 61 LYS CB C 33.10 . . 712 61 LYS HB2 H 1.77 . . 713 61 LYS HB3 H 1.93 . . 714 61 LYS HG2 H 1.42 . . 715 61 LYS HG3 H 1.45 . . 716 61 LYS HD2 H 1.96 . . 717 61 LYS HD3 H 1.79 . . 718 61 LYS CG C 24.50 . . 719 61 LYS CD C 28.80 . . 720 62 ARG N N 121.41 . . 721 62 ARG H H 9.51 . . 722 62 ARG C C 177.37 . . 723 62 ARG CA C 60.50 . . 724 62 ARG HA H 3.76 . . 725 62 ARG CB C 33.60 . . 726 62 ARG HB2 H 2.17 . . 727 62 ARG HB3 H 2.17 . . 728 62 ARG HG2 H 1.46 . . 729 62 ARG HG3 H 1.64 . . 730 62 ARG CG C 26.60 . . 731 63 ALA N N 118.41 . . 732 63 ALA H H 7.60 . . 733 63 ALA C C 180.57 . . 734 63 ALA CA C 54.90 . . 735 63 ALA HA H 4.30 . . 736 63 ALA CB C 17.70 . . 737 63 ALA HB H 1.60 . . 738 64 ALA N N 120.51 . . 739 64 ALA H H 7.73 . . 740 64 ALA C C 179.17 . . 741 64 ALA CA C 54.90 . . 742 64 ALA HA H 4.30 . . 743 64 ALA CB C 18.00 . . 744 64 ALA HB H 1.64 . . 745 65 TYR N N 120.81 . . 746 65 TYR H H 8.99 . . 747 65 TYR C C 178.67 . . 748 65 TYR CA C 61.30 . . 749 65 TYR HA H 4.18 . . 750 65 TYR CB C 39.10 . . 751 65 TYR HB2 H 3.09 . . 752 65 TYR HB3 H 3.23 . . 753 65 TYR HD1 H 7.04 . . 754 65 TYR HD2 H 7.04 . . 755 65 TYR HE1 H 6.36 . . 756 65 TYR HE2 H 6.36 . . 757 65 TYR CD1 C 133.30 . . 758 65 TYR CD2 C 133.30 . . 759 65 TYR CE1 C 118.90 . . 760 65 TYR CE2 C 118.90 . . 761 66 ASP N N 120.61 . . 762 66 ASP H H 9.33 . . 763 66 ASP C C 177.37 . . 764 66 ASP CA C 56.80 . . 765 66 ASP HA H 4.41 . . 766 66 ASP CB C 39.80 . . 767 66 ASP HB2 H 2.66 . . 768 66 ASP HB3 H 2.83 . . 769 67 GLN N N 116.91 . . 770 67 GLN H H 7.57 . . 771 67 GLN C C 176.87 . . 772 67 GLN CA C 57.70 . . 773 67 GLN HA H 4.07 . . 774 67 GLN CB C 29.40 . . 775 67 GLN HB2 H 1.48 . . 776 67 GLN HB3 H 1.76 . . 777 67 GLN HG2 H 1.63 . . 778 67 GLN HG3 H 1.98 . . 779 67 GLN HE21 H 6.69 . . 780 67 GLN HE22 H 7.10 . . 781 67 GLN CG C 33.10 . . 782 67 GLN NE2 N 110.20 . . 783 68 TYR N N 114.91 . . 784 68 TYR H H 8.44 . . 785 68 TYR C C 176.47 . . 786 68 TYR CA C 57.40 . . 787 68 TYR HA H 4.72 . . 788 68 TYR CB C 40.10 . . 789 68 TYR HB2 H 2.71 . . 790 68 TYR HB3 H 3.14 . . 791 68 TYR HD1 H 7.19 . . 792 68 TYR HD2 H 7.19 . . 793 68 TYR HE1 H 6.79 . . 794 68 TYR HE2 H 6.79 . . 795 68 TYR CD1 C 133.50 . . 796 68 TYR CD2 C 133.50 . . 797 68 TYR CE1 C 118.40 . . 798 68 TYR CE2 C 118.40 . . 799 69 GLY N N 110.61 . . 800 69 GLY H H 8.49 . . 801 69 GLY C C 174.17 . . 802 69 GLY CA C 45.10 . . 803 69 GLY HA2 H 3.30 . . 804 69 GLY HA3 H 3.97 . . 805 70 HIS N N 118.91 . . 806 70 HIS H H 8.58 . . 807 70 HIS C C 175.77 . . 808 70 HIS CA C 59.00 . . 809 70 HIS HA H 4.53 . . 810 70 HIS CB C 29.60 . . 811 70 HIS HB2 H 3.17 . . 812 70 HIS HB3 H 3.30 . . 813 70 HIS HD2 H 7.22 . . 814 70 HIS CD2 C 119.40 . . 815 71 ALA N N 121.11 . . 816 71 ALA H H 8.20 . . 817 71 ALA C C 178.07 . . 818 71 ALA CA C 53.80 . . 819 71 ALA HA H 4.22 . . 820 71 ALA CB C 18.30 . . 821 71 ALA HB H 1.47 . . 822 72 ALA N N 118.61 . . 823 72 ALA H H 7.75 . . 824 72 ALA C C 177.37 . . 825 72 ALA CA C 53.40 . . 826 72 ALA HA H 3.92 . . 827 72 ALA CB C 18.40 . . 828 72 ALA HB H 1.00 . . 829 73 PHE N N 114.91 . . 830 73 PHE H H 7.67 . . 831 73 PHE C C 175.67 . . 832 73 PHE CA C 56.60 . . 833 73 PHE HA H 4.77 . . 834 73 PHE CB C 39.40 . . 835 73 PHE HB2 H 3.01 . . 836 73 PHE HB3 H 3.47 . . 837 73 PHE HD1 H 7.39 . . 838 73 PHE HD2 H 7.39 . . 839 73 PHE CD1 C 132.30 . . 840 73 PHE CD2 C 132.30 . . 841 74 GLU N N 120.11 . . 842 74 GLU H H 7.72 . . 843 74 GLU C C 176.27 . . 844 74 GLU CA C 56.20 . . 845 74 GLU HA H 4.36 . . 846 74 GLU CB C 30.30 . . 847 74 GLU HB2 H 1.96 . . 848 74 GLU HB3 H 2.11 . . 849 74 GLU HG2 H 2.32 . . 850 74 GLU HG3 H 2.37 . . 851 74 GLU CG C 35.80 . . 852 75 GLN N N 120.31 . . 853 75 GLN H H 8.52 . . 854 75 GLN CA C 56.10 . . 855 75 GLN HA H 4.31 . . 856 75 GLN CB C 29.30 . . 857 75 GLN HB2 H 2.03 . . 858 75 GLN HB3 H 2.13 . . 859 75 GLN HG2 H 2.39 . . 860 75 GLN HG3 H 2.39 . . 861 75 GLN HE21 H 7.57 . . 862 75 GLN HE22 H 6.82 . . 863 75 GLN CG C 33.60 . . 864 75 GLN NE2 N 112.00 . . 865 76 GLY CA C 45.20 . . 866 76 GLY HA2 H 3.97 . . 867 77 GLY CA C 46.00 . . 868 77 GLY HA2 H 3.76 . . 869 78 MET N N 118.91 . . 870 78 MET H H 8.32 . . 871 78 MET CA C 55.50 . . 872 78 MET HA H 4.45 . . 873 78 MET CB C 32.30 . . 874 78 MET HB2 H 2.02 . . 875 78 MET HB3 H 2.16 . . 876 78 MET HG2 H 2.54 . . 877 78 MET HG3 H 2.00 . . 878 78 MET HE H 2.02 . . 879 78 MET CE C 16.70 . . 880 83 PHE N N 119.61 . . 881 83 PHE H H 8.20 . . 882 83 PHE CA C 57.70 . . 883 83 PHE HA H 4.47 . . 884 86 GLY CA C 45.10 . . 885 86 GLY HA2 H 3.31 . . 886 87 ALA N N 123.51 . . 887 87 ALA H H 8.36 . . 888 87 ALA CA C 52.50 . . 889 87 ALA HA H 4.36 . . 890 87 ALA CB C 19.00 . . 891 87 ALA HB H 1.41 . . 892 88 ASP N N 118.71 . . 893 88 ASP H H 8.38 . . 894 88 ASP C C 174.87 . . 895 88 ASP CA C 54.10 . . 896 88 ASP HA H 4.64 . . 897 88 ASP CB C 41.00 . . 898 88 ASP HB2 H 2.75 . . 899 88 ASP HB3 H 2.75 . . 900 89 PHE C C 174.37 . . 901 89 PHE CA C 57.70 . . 902 89 PHE HA H 4.47 . . 903 89 PHE CB C 40.10 . . 904 89 PHE HB2 H 2.96 . . 905 89 PHE HB3 H 3.18 . . 906 90 SER N N 116.91 . . 907 90 SER H H 8.43 . . 908 90 SER CA C 58.30 . . 909 90 SER HA H 4.48 . . 910 90 SER CB C 63.60 . . 911 90 SER HB2 H 3.89 . . 912 90 SER HB3 H 3.95 . . 913 91 ASP N N 115.51 . . 914 91 ASP H H 8.24 . . 915 91 ASP C C 175.97 . . 916 91 ASP CA C 54.10 . . 917 91 ASP HA H 4.64 . . 918 91 ASP CB C 41.00 . . 919 91 ASP HB2 H 2.75 . . 920 91 ASP HB3 H 2.75 . . 921 92 ILE N N 118.91 . . 922 92 ILE H H 7.89 . . 923 92 ILE CA C 61.30 . . 924 92 ILE HA H 4.12 . . 925 92 ILE CB C 38.60 . . 926 92 ILE HB H 1.80 . . 927 92 ILE HG12 H 0.81 . . 928 92 ILE HG13 H 0.81 . . 929 92 ILE HG2 H 0.76 . . 930 92 ILE HD1 H 0.81 . . 931 92 ILE CG1 C 20.80 . . 932 92 ILE CG2 C 17.20 . . 933 92 ILE CD1 C 12.80 . . 934 93 PHE N N 121.91 . . 935 93 PHE H H 8.21 . . 936 93 PHE CA C 57.70 . . 937 93 PHE HA H 4.65 . . 938 93 PHE CB C 39.40 . . 939 93 PHE HB2 H 3.26 . . 940 93 PHE HB3 H 3.02 . . 941 95 ASP N N 120.01 . . 942 95 ASP H H 8.25 . . 943 95 ASP C C 176.17 . . 944 95 ASP CA C 54.10 . . 945 95 ASP HA H 4.64 . . 946 95 ASP CB C 41.60 . . 947 95 ASP HB2 H 2.57 . . 948 95 ASP HB3 H 2.62 . . 949 96 VAL N N 118.71 . . 950 96 VAL H H 7.98 . . 951 96 VAL C C 175.77 . . 952 96 VAL CA C 62.20 . . 953 96 VAL HA H 4.08 . . 954 96 VAL CB C 32.30 . . 955 96 VAL HB H 2.00 . . 956 96 VAL HG1 H 0.77 . . 957 96 VAL HG2 H 0.83 . . 958 96 VAL CG1 C 20.00 . . 959 96 VAL CG2 C 20.00 . . 960 97 PHE N N 121.91 . . 961 97 PHE H H 8.28 . . 962 97 PHE CA C 57.60 . . 963 97 PHE HA H 4.70 . . 964 97 PHE CB C 39.40 . . 965 97 PHE HB2 H 3.26 . . 966 97 PHE HB3 H 3.02 . . 967 98 GLY N N 109.21 . . 968 98 GLY H H 8.20 . . 969 98 GLY C C 174.27 . . 970 99 ASP N N 121.61 . . 971 99 ASP H H 8.33 . . 972 99 ASP CA C 54.10 . . 973 99 ASP HA H 4.64 . . 974 99 ASP CB C 40.90 . . 975 99 ASP HB2 H 2.66 . . 976 99 ASP HB3 H 2.66 . . 977 100 ILE CA C 61.30 . . 978 100 ILE HA H 4.12 . . 979 100 ILE HG12 H 0.76 . . 980 100 ILE HG13 H 0.76 . . 981 100 ILE HG2 H 0.71 . . 982 100 ILE HD1 H 0.76 . . 983 100 ILE CG1 C 20.90 . . 984 100 ILE CG2 C 17.20 . . 985 100 ILE CD1 C 12.90 . . 986 101 PHE N N 122.31 . . 987 101 PHE H H 8.24 . . 988 101 PHE CA C 57.70 . . 989 101 PHE HA H 4.46 . . 990 101 PHE CB C 40.10 . . 991 101 PHE HB2 H 2.96 . . 992 101 PHE HB3 H 3.18 . . stop_ save_